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     Western blot analysis of FKBP38 expression in Jurkat cell lysate.    

  
  

FKBP38 (FK506-binding protein 38) is a member of the immunophilin protein family, known for its peptidyl-prolyl isomerase (PPIase) activity and involvement in diverse cellular processes. Unlike other FKBP proteins, FKBP38 uniquely localizes to mitochondrial and endoplasmic reticulum membranes, where it interacts with key regulators of apoptosis and autophagy. It binds to Bcl-2 and Bcl-XL, modulating mitochondrial membrane permeability and caspase-dependent cell death. Additionally, FKBP38 regulates mTOR signaling by interacting with Rheb GTPase, influencing cell growth and nutrient response. Its role in neurodevelopment and neurodegeneration, particularly in Alzheimer’s disease via amyloid-beta toxicity pathways, has drawn significant research interest.

FKBP38 antibodies are essential tools for studying these mechanisms. They enable detection and quantification of FKBP38 in tissues or cultured cells through techniques like Western blot, immunofluorescence, and immunoprecipitation. Commercial antibodies are often raised against specific epitopes, such as the N-terminal domain (e.g., amino acids 1-150) or C-terminal regions. Some antibodies distinguish between phosphorylated or ubiquitinated forms, aiding in post-translational modification studies. Validation in knockout models or siRNA-treated samples is critical due to potential cross-reactivity with other FKBPs. Research applications include investigating FKBP38's dual roles in cell survival/death, its interaction with HSP90. and its dysregulation in cancers or neurological disorders. Recent studies also explore its potential as a therapeutic target, particularly in chemotherapy resistance contexts.